ID A0A137Q944_9AGAR Unreviewed; 428 AA.
AC A0A137Q944;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AN958_00858 {ECO:0000313|EMBL:KXN83716.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN83716.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN83716.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN83716.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; KQ962764; KXN83716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137Q944; -.
DR STRING; 1714833.A0A137Q944; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF35; CYSTATHIONINE GAMMA-SYNTHASE (AFU_ORTHOLOGUE AFUA_7G01590); 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT MOD_RES 225
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 428 AA; 47039 MW; 29CEC03C4CFB5BCF CRC64;
MASKENDRLS GTDLIHGDSR VPYFKGAGGA VAPSISVSTT FRSAAPDEGA IPYTEVDLRN
PERHVYSRYT QEASSRAEHV LSKVLNGYAL TYASGLNAVY AVSCSFGTIK IDHQLTLVIK
ALVHYQPKRI AVREGYHGCH QCVAIYRRSC PEVEVIDIDA DFKAGDLCWI ETPLNPYGIC
RDIQHYADKI HKVGGILAVD STFGPPPLQD PFKFGADCIM HSGTKYFGGH SDLLCGVLVV
KTEEEWRKLH HDRTYLGCPM GSLEAWLLLR SLKTLHLRVP RQSQTATALA KWLDSLSKVP
EGQTIEGISA GLVTRVWHSS LQGTDARGFN PQDQMPGGFN STFSVELATI ELASRLPHLL
EFFVPATSLG GVESLVEHRL GSDPGADPTI VRLSIGVEEF EDLKADLRQA LQKLDKVRYS
VLFFSLSG
//